Abnormalities in cellular protein folding play a crucial role in many pathological conditions such as Alzheimers, cancer, and ischemia. The chaperonin system Tric plays a pivotal role in cellular protein folding. We propose to study the mammalian chaperone system Tric using small angle x-ray scattering (SAXS) and compare it with its bacterial counterpart, the GroEL system. In the first phase of our study, we will perform a series of static and time-resolved measurements on the GroEL system. While a number of open questions remain concerning this system, GroEL is reasonably well characterized and will serve as a model in our work. Static and time-resolved work on the eukaryotic system Tric will comprise the bulk of our effort. The large conformational changes we expect with this chaperone system are best observed with SAXS and will likely provide important insights into this chaperone complex.